The UBR5 antibody is a key tool for studying the ubiquitin-protein ligase E3 component N-recognin 5 (UBR5), a member of the HECT-domain E3 ubiquitin ligase family. UBR5 plays a critical role in ubiquitination, a post-translational modification that tags proteins for degradation via the proteasome or alters their cellular functions. It is involved in diverse processes, including DNA damage response, cell cycle regulation, and apoptosis. UBR5 has been implicated in cancer, with studies showing both tumor-suppressive and oncogenic roles depending on context, as well as in neurological disorders and metabolic regulation.
UBR5 antibodies are widely used in techniques like Western blotting, immunohistochemistry, and immunofluorescence to detect UBR5 expression levels, localization, and interactions in cells or tissues. Researchers employ these antibodies to explore UBR5's regulatory mechanisms, such as its involvement in degrading substrates like XIAP or modulating signaling pathways like Hippo. Commercial UBR5 antibodies are typically validated for specificity against conserved regions of the protein, though variability in isoforms (e.g., due to alternative splicing) requires careful experimental design. Recent studies highlight UBR5's therapeutic potential, driving demand for reliable antibodies to advance mechanistic and translational research in diseases like breast cancer, glioblastoma, and obesity-linked conditions.